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Y1112_STRPN
ID   Y1112_STRPN             Reviewed;         279 AA.
AC   Q97QT7;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=DegV domain-containing protein SP_1112;
GN   OrderedLocusNames=SP_1112;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and may
CC       play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q97QT7; A0A0H2UPN3: SP_0859; NbExp=2; IntAct=EBI-6474517, EBI-6474523;
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DR   EMBL; AE005672; AAK75223.1; -; Genomic_DNA.
DR   PIR; F95128; F95128.
DR   RefSeq; WP_000161399.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97QT7; -.
DR   SMR; Q97QT7; -.
DR   IntAct; Q97QT7; 1.
DR   STRING; 170187.SP_1112; -.
DR   EnsemblBacteria; AAK75223; AAK75223; SP_1112.
DR   KEGG; spn:SP_1112; -.
DR   eggNOG; COG1307; Bacteria.
DR   OMA; EIHAKIN; -.
DR   PhylomeDB; Q97QT7; -.
DR   BioCyc; SPNE170187:G1FZB-1137-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1180.10; -; 1.
DR   InterPro; IPR003797; DegV.
DR   InterPro; IPR043168; DegV_C.
DR   Pfam; PF02645; DegV; 1.
DR   TIGRFAMs; TIGR00762; DegV; 1.
DR   PROSITE; PS51482; DEGV; 1.
PE   1: Evidence at protein level;
KW   Lipid-binding.
FT   CHAIN           1..279
FT                   /note="DegV domain-containing protein SP_1112"
FT                   /id="PRO_0000209795"
FT   DOMAIN          4..277
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         62
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT   BINDING         94
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ   SEQUENCE   279 AA;  30658 MW;  767394119DC89CAE CRC64;
     MTKIKIVTDS SVTIEPELVK QLDITIVPLS VMIDNVVYSD ADLKEEGKFL QLMQESKNLP
     KTSQPPVGVF AEIFEDLCKD GGQILAIHMS HALSGTVEAA RQGASLSTAD VTVVDSSFTD
     QALKFQVVEA AKLAQEGKDM EAILSHVEEV KNHTELYIGV STLENLVKGG RISRVTGLLS
     SLLNIRAVMQ MKDHELQPMV KGRGTKTFKK WLDELITSLS ERAVAEIGIS YSGSDDWAKE
     MKESLQAYVE KPISVLETGS IIQTHTGENA WAILIRYHS
 
 
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